Recombinant Human TRIM27 Protein, N-His

Description of Recombinant Human TRIM27 Protein, N-His

Introduction

Recombinant Human TRIM27 Protein, also known as Tripartite Motif Containing 27, is a protein that plays a crucial role in the regulation of various cellular processes. It is a member of the tripartite motif (TRIM) family, which is characterized by a conserved domain structure consisting of a RING finger, one or two B-box domains, and a coiled-coil region. The TRIM family is involved in a wide range of cellular functions, including protein degradation, transcriptional regulation, and antiviral defense. In this article, we will discuss the structure, activity, and applications of Recombinant Human TRIM27 Protein.

Structure of Recombinant Human TRIM27 Protein

Recombinant Human TRIM27 Protein is a 61 kDa protein consisting of 535 amino acids. It is composed of four distinct domains: a RING finger domain, two B-box domains, a coiled-coil domain, and a C-terminal PRY/SPRY domain. The RING finger domain is responsible for E3 ubiquitin ligase activity, which is essential for protein degradation and regulation of cellular processes. The B-box domains are involved in protein-protein interactions, while the coiled-coil domain is responsible for the formation of homodimers or heterodimers with other TRIM family members. The C-terminal PRY/SPRY domain is involved in protein-protein interactions and has been linked to the regulation of innate immune signaling.

Activity of Recombinant Human TRIM27 Protein

Recombinant Human TRIM27 Protein has been shown to have multiple activities in various cellular processes. One of its main functions is the regulation of protein degradation through the E3 ubiquitin ligase activity of its RING finger domain. This activity allows TRIM27 to target specific proteins for degradation, thereby regulating their levels and functions in the cell. Additionally, TRIM27 has been shown to play a role in transcriptional regulation by interacting with transcription factors and modulating their activity.

Moreover, Recombinant Human TRIM27 Protein has been linked to the regulation of innate immune signaling. The PRY/SPRY domain of TRIM27 has been shown to interact with viral proteins and activate the innate immune response, leading to the production of antiviral cytokines. This activity of TRIM27 is crucial in the defense against viral infections.

Applications of Recombinant Human TRIM27 Protein

Due to its diverse activities, Recombinant Human TRIM27 Protein has various potential applications in both research and therapeutics. Its role in protein degradation makes it a valuable tool for studying the regulation of cellular processes. Researchers can use Recombinant Human TRIM27 Protein to target specific proteins for degradation and study the effects on cellular functions.

Moreover, the innate immune signaling activity of TRIM27 makes it a potential target for antiviral therapeutics. By activating the innate immune response, Recombinant Human TRIM27 Protein can help in the defense against viral infections. This activity can also be utilized in the development of vaccines against viral diseases.

Additionally, the interaction of TRIM27 with transcription factors makes it a potential target for the treatment of diseases related to transcriptional dysregulation, such as cancer. By modulating the activity of these transcription factors, Recombinant Human TRIM27 Protein can potentially regulate the expression of genes involved in cancer progression.

Conclusion

In summary, Recombinant Human TRIM27 Protein is a multifunctional protein with diverse activities in various cellular processes. Its structure, consisting of a RING finger domain, two B-box domains, a coiled-coil domain, and a C-terminal PRY/SPRY domain, allows it to perform its functions effectively. Recombinant Human TRIM27 Protein has potential applications in research and therapeutics, making it a valuable tool in the scientific community. Further studies on this protein may uncover more functions and potential applications, making it an exciting area of research.